Evidence map›Paper›PMID 26618221›Full record

ArticleJournal of the American Chemical Society2015

Single Enzyme Experiments Reveal a Long-Lifetime Proton Leak State in a Heme-Copper Oxidase.

Mengqiu Li, Sune K Jørgensen, Duncan G G McMillan, Łukasz Krzemiński, Nikolaos N Daskalakis, Riitta H Partanen, Marijonas Tutkus, Roman Tuma, Dimitrios Stamou, Nikos S Hatzakis and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 44 citations in OpenAlex.

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  11. Constructing artificial respiratory chain in polymer compartments: Insights into the interplay betweenProceedings of the National Academy of Sciences of the United States of America · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Mengqiu LiSchool of Biomedical Sciences, University of Leeds , LS2 9JT Leeds, U.K.
Sune K JørgensenDepartment of Chemistry, Nano-Science Center and Lundbeck Foundation Center for Biomembranes in Nanomedicine, University of Copenhagen , 2100 Copenhagen, Denmark.
Duncan G G McMillanSchool of Biomedical Sciences, University of Leeds , LS2 9JT Leeds, U.K.
Łukasz KrzemińskiSchool of Biomedical Sciences, University of Leeds , LS2 9JT Leeds, U.K.
Nikolaos N DaskalakisSchool of Biomedical Sciences, University of Leeds , LS2 9JT Leeds, U.K.
Riitta H PartanenSchool of Biomedical Sciences, University of Leeds , LS2 9JT Leeds, U.K.
Marijonas TutkusDepartment of Chemistry, Nano-Science Center and Lundbeck Foundation Center for Biomembranes in Nanomedicine, University of Copenhagen , 2100 Copenhagen, Denmark.
Roman TumaSchool of Molecular and Cellular Biology, University of Leeds , LS2 9JT Leeds, U.K.
Dimitrios StamouDepartment of Chemistry, Nano-Science Center and Lundbeck Foundation Center for Biomembranes in Nanomedicine, University of Copenhagen , 2100 Copenhagen, Denmark.
Nikos S HatzakisDepartment of Chemistry, Nano-Science Center and Lundbeck Foundation Center for Biomembranes in Nanomedicine, University of Copenhagen , 2100 Copenhagen, Denmark.
Lars J C JeukenSchool of Biomedical Sciences, University of Leeds , LS2 9JT Leeds, U.K.
Lundbeck Foundation · DKUniversity of Copenhagen · DK

Funding

European Research Council 280518
6 · The paper itself

Abstract

Heme-copper oxidases (HCOs) are key enzymes in prokaryotes and eukaryotes for energy production during aerobic respiration. They catalyze the reduction of the terminal electron acceptor, oxygen, and utilize the Gibbs free energy to transport protons across a membrane to generate a proton (ΔpH) and electrochemical gradient termed proton motive force (PMF), which provides the driving force for the adenosine triphosphate (ATP) synthesis. Excessive PMF is known to limit the turnover of HCOs, but the molecular mechanism of this regulatory feedback remains relatively unexplored. Here we present a single-enzyme study that reveals that cytochrome bo3 from Escherichia coli, an HCO closely homologous to Complex IV in human mitochondria, can enter a rare, long-lifetime leak state during which proton flow is reversed. The probability of entering the leak state is increased at higher ΔpH. By rapidly dissipating the PMF, we propose that this leak state may enable cytochrome bo3, and possibly other HCOs, to maintain a suitable ΔpH under extreme redox conditions.

Identifiers

PMID26618221
PMCPMC4697922
OpenAlexW2182889776

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.